Calcium-binding EGF-like modules in coagulation proteinases: function of the calcium ion in module interactions.

[1]  E. Thulin,et al.  EGF-like module pair 3-4 in vitamin K-dependent protein S: modulation of calcium affinity of module 4 by module 3, and interaction with factor X. , 1999, Journal of molecular biology.

[2]  T. Darden,et al.  Probing the structural changes in the light chain of human coagulation factor VIIa due to tissue factor association. , 1999, Biophysical journal.

[3]  R. Kelley,et al.  The effect of O-fucosylation on the first EGF-like domain from human blood coagulation factor VII. , 1999, Biochemistry.

[4]  A. Holder,et al.  Solution structure of an EGF module pair from the Plasmodium falciparum merozoite surface protein 1. , 1999, Journal of molecular biology.

[5]  S. Artavanis-Tsakonas,et al.  Notch signaling: cell fate control and signal integration in development. , 1999, Science.

[6]  N. Thielens,et al.  The N-terminal CUB-Epidermal Growth Factor Module Pair of Human Complement Protease C1r Binds Ca2+ with High Affinity and Mediates Ca2+-dependent Interaction with C1s* , 1999, The Journal of Biological Chemistry.

[7]  P. Handford,et al.  EGF-like domain calcium affinity modulated by N-terminal domain linkage in human fibrillin-1. , 1999, Journal of molecular biology.

[8]  P. Handford,et al.  Defective calcium binding to fibrillin-1: consequence of an N2144S change for fibrillin-1 structure and function. , 1999, Journal of molecular biology.

[9]  S. Kent,et al.  Chemical synthesis of human protein S thrombin-sensitive module and first epidermal growth factor module. , 1998, Biopolymers.

[10]  G. Gippert,et al.  Solution structure of the N-terminal EGF-like domain from human factor VII. , 1998, Biochemistry.

[11]  I. Campbell,et al.  NMR of modular proteins , 1998, Nature Structural Biology.

[12]  P. Handford,et al.  A Gly → Ser Change Causes Defective Folding in Vitro of Calcium-binding Epidermal Growth Factor-like Domains from Factor IX and Fibrillin-1* , 1998, The Journal of Biological Chemistry.

[13]  D. Marion,et al.  Solution structure of the epidermal growth factor (EGF)-like module of human complement protease C1r, an atypical member of the EGF family. , 1998, Biochemistry.

[14]  B. Dahlbäck,et al.  Characterization of recombinant epidermal growth factor (EGF)-like modules from vitamin-K-dependent protein S expressed in Spodoptera cells--the cofactor activity depends on the N-terminal EGF module in human protein S. , 1998, European journal of biochemistry.

[15]  O. Christophe,et al.  Blood Coagulation Factor IX Residues Glu78 and Arg94 Provide a Link between Both Epidermal Growth Factor-like Domains That Is Crucial in the Interaction with Factor VIII Light Chain* , 1998, The Journal of Biological Chemistry.

[16]  B. Villoutreix,et al.  Calcium binding to tandem repeats of EGF‐like modules. Expression and characterization of the EGF‐like modules of human Notch‐1 implicated in receptor‐ligand interactions , 1997, Protein science : a publication of the Protein Society.

[17]  S. Linse,et al.  The High Affinity Calcium-binding Sites in the Epidermal Growth Factor Module Region of Vitamin K-dependent Protein S* , 1997, The Journal of Biological Chemistry.

[18]  T. Drakenberg,et al.  Calcium-binding properties of the third and fourth epidermal-growth-factor-like modules in vitamin-K-dependent protein S. , 1997, European journal of biochemistry.

[19]  W. Ruf,et al.  Ca2+ Binding to the First Epidermal Growth Factor Module of Coagulation Factor VIIa Is Important for Cofactor Interaction and Proteolytic Function* , 1997, The Journal of Biological Chemistry.

[20]  T. Edgington,et al.  The Structural Basis of Function of the TF●VIIa Complex in the Cellular Initiation of Coagulation , 1997, Thrombosis and Haemostasis.

[21]  S Foundling,et al.  The 2.8 A crystal structure of Gla‐domainless activated protein C. , 1996, The EMBO journal.

[22]  J. Trewhella,et al.  The relative orientation of Gla and EGF domains in coagulation factor X is altered by Ca2+ binding to the first EGF domain. A combined NMR-small angle X-ray scattering study. , 1996, Biochemistry.

[23]  I. Campbell,et al.  Solution Structure of a Pair of Calcium-Binding Epidermal Growth Factor-like Domains: Implications for the Marfan Syndrome and Other Genetic Disorders , 1996, Cell.

[24]  P Bork,et al.  Structure and distribution of modules in extracellular proteins , 1996, Quarterly Reviews of Biophysics.

[25]  David W. Banner,et al.  The crystal structure of the complex of blood coagulation factor VIIa with soluble tissue factor , 1996, Nature.

[26]  P. Handford,et al.  Calcium binding properties of an epidermal growth factor-like domain pair from human fibrillin-1. , 1996, Journal of molecular biology.

[27]  P. Handford,et al.  The structure of a Ca2+-binding epidermal growth factor-like domain: Its role in protein-protein interactions , 1995, Cell.

[28]  S. Forsén,et al.  Structure of the Ca2+-free GLA domain sheds light on membrane binding of blood coagulation proteins , 1995, Nature Structural Biology.

[29]  P. Handford,et al.  The Calcium Binding Properties and Molecular Organization of Epidermal Growth Factor-like Domains in Human Fibrillin-1 (*) , 1995, The Journal of Biological Chemistry.

[30]  R. Glanville,et al.  Calcium binding, hydroxylation, and glycosylation of the precursor epidermal growth factor-like domains of fibrillin-1, the Marfan gene protein. , 1994, The Journal of biological chemistry.

[31]  A. Holmgren,et al.  Calcium-dependent interaction between gamma-carboxyglutamic acid-containing and N-terminal epidermal growth factor-like modules in factor X. , 1994, The Journal of biological chemistry.

[32]  M. Ullner,et al.  How an epidermal growth factor (EGF)-like domain binds calcium. High resolution NMR structure of the calcium form of the NH2-terminal EGF-like domain in coagulation factor X. , 1994, The Journal of biological chemistry.

[33]  P. Loll,et al.  The X-ray crystal structure of the membrane protein prostaglandin H2 synthase-1 , 1994, Nature.

[34]  C. Kielty,et al.  The role of calcium in the organization of fibrillin microfibrils , 1993, FEBS letters.

[35]  J. Stenflo,et al.  Calcium affinity of the NH2-terminal epidermal growth factor-like module of factor X. Effect of the gamma-carboxyglutamic acid-containing module. , 1993, The Journal of biological chemistry.

[36]  I. Campbell,et al.  The effect of aspartate hydroxylation on calcium binding to epidermal growth factor-like modules in coagulation factors IX and X. , 1993, The Journal of biological chemistry.

[37]  P. Handford,et al.  Tyrosine 69 of the first epidermal growth factor-like domain of human factor IX is essential for clotting activity. , 1993, The Journal of biological chemistry.

[38]  R. Huber,et al.  Structure of human des(1-45) factor Xa at 2.2 A resolution. , 1993, Journal of molecular biology.

[39]  R F Doolittle,et al.  The Evolution of Vertebrate Blood Coagulation: A Case of Yin and Yang , 1993, Thrombosis and Haemostasis.

[40]  P. Bork,et al.  Epidermal growth factor-like modules , 1993 .

[41]  Reed J. Harris,et al.  O-linked fucose and other post-translational modifications unique to EGF modules. , 1993, Glycobiology.

[42]  K. O. Elliston,et al.  cDNA cloning and expression of bovine aspartyl (asparaginyl) beta-hydroxylase. , 1992, The Journal of biological chemistry.

[43]  T. Drakenberg,et al.  Three-dimensional structure of the apo form of the N-terminal EGF-like module of blood coagulation factor X as determined by NMR spectroscopy and simulated folding. , 1992, Biochemistry.

[44]  C. Esmon,et al.  The high affinity calcium-binding site involved in protein C activation is outside the first epidermal growth factor homology domain. , 1992, The Journal of biological chemistry.

[45]  I. Campbell,et al.  Solution structure of the fifth repeat of factor H: a second example of the complement control protein module. , 1992, Biochemistry.

[46]  I. Campbell,et al.  The three‐dimensional structure of the first EGF‐like module of human factor IX: Comparison with EGF and TGF‐α , 1992, Protein science : a publication of the Protein Society.

[47]  G. Long,et al.  beta-Hydroxyaspartic acid and beta-hydroxyasparagine residues in recombinant human protein S are not required for anticoagulant cofactor activity or for binding to C4b-binding protein. , 1991, The Journal of biological chemistry.

[48]  J. Stenflo,et al.  Structure-function relationships of epidermal growth factor modules in vitamin K-dependent clotting factors. , 1991, Blood.

[49]  R. Glanville,et al.  Partial sequence of a candidate gene for the Marfan syndrome , 1991, Nature.

[50]  M. Mattei,et al.  Linkage of Marfan syndrome and a phenotypically related disorder to two different fibrillin genes , 1991, Nature.

[51]  W. Kisiel,et al.  Human plasma and recombinant factor VII. Characterization of O-glycosylations at serine residues 52 and 60 and effects of site-directed mutagenesis of serine 52 to alanine. , 1991, The Journal of biological chemistry.

[52]  László Patthy,et al.  Modular exchange principles in proteins , 1991 .

[53]  I. D. Campbell,et al.  Key residues involved in calcium-binding motifs in EGF-like domains , 1991, Nature.

[54]  J. Stenflo,et al.  Protein structural requirements for Ca2+ binding to the light chain of factor X. Studies using isolated intact fragments containing the gamma-carboxyglutamic acid region and/or the epidermal growth factor-like domains. , 1991, The Journal of biological chemistry.

[55]  B. Dahlbäck,et al.  Novel type of very high affinity calcium-binding sites in beta-hydroxyasparagine-containing epidermal growth factor-like domains in vitamin K-dependent protein S. , 1990, The Journal of biological chemistry.

[56]  J. Stenflo,et al.  sup 1 H NMR assignment and secondary structure of the Ca sup 2+ -free form of the amino-terminal epidermal growth factor like domain in coagulation factor X , 1990 .

[57]  D. Monroe,et al.  Characterization of the functional defect in factor IX Alabama. Evidence for a conformational change due to high affinity calcium binding in the first epidermal growth factor domain. , 1990, The Journal of biological chemistry.

[58]  V. Garsky,et al.  Partial purification and characterization of bovine liver aspartyl beta-hydroxylase. , 1990, The Journal of biological chemistry.

[59]  W. Kisiel,et al.  Identification of a disaccharide (Xyl-Glc) and a trisaccharide (Xyl2-Glc) O-glycosidically linked to a serine residue in the first epidermal growth factor-like domain of human factors VII and IX and protein Z and bovine protein Z. , 1989, The Journal of biological chemistry.

[60]  S. Linse,et al.  Calcium binding to the isolated beta-hydroxyaspartic acid-containing epidermal growth factor-like domain of bovine factor X. , 1989, The Journal of biological chemistry.

[61]  J. Engel.  EGF‐like domains in extracellular matrix proteins: Localized signals for growth and differentiation? , 1989, FEBS letters.

[62]  K. Berkner,et al.  Inhibitors of 2-ketoglutarate-dependent dioxygenases block aspartyl beta-hydroxylation of recombinant human factor IX in several mammalian expression systems. , 1989, The Journal of biological chemistry.

[63]  S. Kawabata,et al.  A new trisaccharide sugar chain linked to a serine residue in bovine blood coagulation factors VII and IX. , 1988, Journal of biochemistry.

[64]  L. Thim,et al.  Amino acid sequence and posttranslational modifications of human factor VIIa from plasma and transfected baby hamster kidney cells. , 1988, Biochemistry.

[65]  P. Handford,et al.  The role of beta‐hydroxyaspartate and adjacent carboxylate residues in the first EGF domain of human factor IX. , 1988, The EMBO journal.

[66]  S. Linse,et al.  Calcium binding to the epidermal growth factor homology region of bovine protein C. , 1988, The Journal of biological chemistry.

[67]  B. Furie,et al.  The molecular basis of blood coagulation , 1988, Cell.

[68]  W. Schneider,et al.  beta-Hydroxyaspartic acid or beta-hydroxyasparagine in bovine low density lipoprotein receptor and in bovine thrombomodulin. , 1988, The Journal of biological chemistry.

[69]  J. Stenflo,et al.  Calcium-dependent interaction between the epidermal growth factor precursor-like region of human protein C and a monoclonal antibody. , 1987, The Journal of biological chemistry.

[70]  C. Esmon,et al.  The active site of blood coagulation factor Xa. Its distance from the phospholipid surface and its conformational sensitivity to components of the prothrombinase complex. , 1987, The Journal of biological chemistry.

[71]  Richard G. W. Anderson,et al.  Acid-dependent ligand dissociation and recycling of LDL receptor mediated by growth factor homology region , 1987, Nature.

[72]  F. Blasi,et al.  Urokinase-type plasminogen activator: proenzyme, receptor, and inhibitors , 1987, The Journal of cell biology.

[73]  L. Patthy.  Evolution of the proteases of blood coagulation and fibrinolysis by assembly from modules , 1985, Cell.

[74]  T. Südhof,et al.  The LDL receptor gene: a mosaic of exons shared with different proteins. , 1985, Science.

[75]  P. Fernlund,et al.  β‐Hydroxyaspartic acid in vitamin K‐dependent plasma proteins from scorbutic and warfarin‐treated guinea pigs , 1984 .

[76]  P. Fernlund,et al.  Beta-hydroxyaspartic acid in vitamin K-dependent proteins. , 1983, The Journal of biological chemistry.

[77]  A. M. Soderquist,et al.  EPIDERMAL GROWTH FACTOR * , 1982, Annals of the New York Academy of Sciences.

[78]  Kenji Matsuno,et al.  Notch signaling. , 1995, Science.

[79]  L. Patthy.  Modular design of proteases of coagulation, fibrinolysis, and complement activation: implications for protein engineering and structure-function studies. , 1993, Methods in enzymology.

[80]  J. Astermark,et al.  Isolation of intact modules from noncatalytic parts of vitamin K-dependent coagulation factors IX and X and protein C. , 1993, Methods in enzymology.

[81]  I. Campbell,et al.  The solution structure of human epidermal growth factor , 1987, Nature.

[82]  J. Ware,et al.  Factor IXAlabama: a point mutation in a clotting protein results in hemophilia B. , 1987, Blood.